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UniProtKB - P50281 (MMP14_HUMAN)

Protein

Matrix metalloproteinase-14

Gene

MMP14

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Endopeptidase that degrades various components of the extracellular matrix such as collagen. Activates progelatinase A. Essential for pericellular collagenolysis and modeling of skeletal and extraskeletal connective tissues during development (By similarity). May be involved in actin cytoskeleton reorganization by cleaving PTK7 (PubMed:20837484). Acts as a positive regulator of cell growth and migration via activation of MMP15. Involved in the formation of the fibrovascular tissues in association with pro-MMP2 (PubMed:12714657). Cleaves ADGRB1 to release vasculostatin-40 which inhibits angiogenesis (PubMed:22330140).By similarity4 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • Endopeptidase activity. Activates progelatinase A by cleavage of the propeptide at 37-Asn-|-Leu-38. Other bonds hydrolyzed include 35-Gly-|-Ile-36 in the propeptide of collagenase 3, and 341-Asn-|-Phe-342, 441-Asp-|-Leu-442 and 354-Gln-|-Thr-355 in the aggrecan interglobular domain. EC:3.4.24.80

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:
  • Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity
  • Ca2+By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi93Zinc; in inhibited formBy similarity1
Metal bindingi239Zinc; catalytic1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei240PROSITE-ProRule annotation1
Metal bindingi243Zinc; catalytic1
Metal bindingi249Zinc; catalytic1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • endopeptidase activity Source: UniProtKB
  • integrin binding Source: Ensembl
  • metalloaminopeptidase activity Source: ParkinsonsUK-UCL
  • metalloendopeptidase activity Source: UniProtKB
  • serine-type endopeptidase activity Source: Reactome
  • zinc ion binding Source: ProtInc
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase, Metalloprotease, Protease
LigandCalcium, Metal-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		MetaCyc:ENSG00000157227-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.4.24.80 2681
3.4.24.B5 2681

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-1442490 Collagen degradation
R-HSA-1474228 Degradation of the extracellular matrix
R-HSA-1592389 Activation of Matrix Metalloproteinases

SIGNOR Signaling Network Open Resource

More...SIGNORi		P50281

Protein family/group databases

MEROPS protease database

More...MEROPSi		M10.014

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Matrix metalloproteinase-14 (EC:3.4.24.80)
Short name:
MMP-14
Alternative name(s):
MMP-X1
Membrane-type matrix metalloproteinase 1
Short name:
MT-MMP 1
Short name:
MTMMP1
Membrane-type-1 matrix metalloproteinase
Short name:
MT1-MMP
Short name:
MT1MMP
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:MMP14
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 14

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000157227.12

Human Gene Nomenclature Database

More...HGNCi		HGNC:7160 MMP14

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		600754 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P50281

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini112 – 541ExtracellularSequence analysisAdd BLAST430
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei542 – 562HelicalSequence analysisAdd BLAST21
Topological domaini563 – 582CytoplasmicSequence analysisAdd BLAST20

Keywords - Cellular componenti

Cytoplasm, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Winchester syndrome (WNCHRS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disease characterized by severe osteolysis in the hands and feet, generalized osteoporosis, bone thinning, and absence of subcutaneous nodules. Various additional features include coarse face, corneal opacities, gum hypertrophy, and EKG changes.
See also OMIM:277950
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_07056717T → R in WNCHRS; results in increased MMP14 proteosomal degradation and reduced protein localization to cell membrane. 1 PublicationCorresponds to variant dbSNP:rs587777039EnsemblClinVar.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...DisGeNETi		4323

MalaCards human disease database

More...MalaCardsi		MMP14
MIMi277950 phenotype

Open Targets

More...OpenTargetsi		ENSG00000157227

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		85196 Nodulosis-arthropathy-osteolysis syndrome
3460 Torg-Winchester syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA30872

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3869

Drug and drug target database

More...DrugBanki		DB00786 Marimastat

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		1638

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		MMP14

Domain mapping of disease mutations (DMDM)

More...DMDMi		317373419

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 20Sequence analysisAdd BLAST20
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000002879821 – 111Activation peptide1 PublicationAdd BLAST91
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000028799112 – 582Matrix metalloproteinase-14Add BLAST471

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi319 ↔ 508By similarity
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei399Phosphotyrosine; by PKDCC1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

The precursor is cleaved by a furin endopeptidase.By similarity
Tyrosine phosphorylated by PKDCC/VLK.1 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Phosphoprotein, Zymogen

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P50281

MaxQB - The MaxQuant DataBase

More...MaxQBi		P50281

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P50281

PeptideAtlas

More...PeptideAtlasi		P50281

PRoteomics IDEntifications database

More...PRIDEi		P50281

ProteomicsDB human proteome resource

More...ProteomicsDBi		56213

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P50281

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P50281

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P50281

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in stromal cells of colon, breast, and head and neck. Expressed in lung tumors.1 Publication

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Up-regulated by NANOS1.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000157227 Expressed in 191 organ(s), highest expression level in endocervix

CleanEx database of gene expression profiles

More...CleanExi		HS_MMP14

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P50281 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P50281 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB009918
HPA051432

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts (via C-terminal cytoplasmic tail) with BST2. Interacts with DLL1; inhibits DLL1-induced Notch signaling (PubMed:21572390).3 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		110466, 20 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P50281

Database of interacting proteins

More...DIPi		DIP-35111N

Protein interaction database and analysis system

More...IntActi		P50281, 43 interactors

Molecular INTeraction database

More...MINTi		P50281

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000308208

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P50281

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1582
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P50281

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P50281

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P50281

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati316 – 364Hemopexin 1Add BLAST49
Repeati365 – 410Hemopexin 2Add BLAST46
Repeati412 – 460Hemopexin 3Add BLAST49
Repeati461 – 508Hemopexin 4Add BLAST48

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi91 – 98Cysteine switchBy similarity8

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the peptidase M10A family.Curated

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1565 Eukaryota
ENOG410XQ5D LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000157808

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000217928

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG052484

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P50281

KEGG Orthology (KO)

More...KOi		K07763

Identification of Orthologs from Complete Genome Data

More...OMAi		NAVMFPW

Database of Orthologous Groups

More...OrthoDBi		EOG091G03DP

Database for complete collections of gene phylogenies

More...PhylomeDBi		P50281

TreeFam database of animal gene trees

More...TreeFami		TF352396

Family and domain databases

Conserved Domains Database

More...CDDi		cd00094 HX, 1 hit
cd04278 ZnMc_MMP, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.101.10, 1 hit
2.110.10.10, 1 hit
3.40.390.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR000585 Hemopexin-like_dom
IPR036375 Hemopexin-like_dom_sf
IPR018487 Hemopexin-like_repeat
IPR018486 Hemopexin_CS
IPR033739 M10A_MMP
IPR024079 MetalloPept_cat_dom_sf
IPR028693 MMP14
IPR001818 Pept_M10_metallopeptidase
IPR021190 Pept_M10A
IPR021805 Pept_M10A_metallopeptidase_C
IPR021158 Pept_M10A_Zn_BS
IPR006026 Peptidase_Metallo
IPR002477 Peptidoglycan-bd-like
IPR036365 PGBD-like_sf
IPR036366 PGBDSf

The PANTHER Classification System

More...PANTHERi		PTHR10201:SF24 PTHR10201:SF24, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF11857 DUF3377, 1 hit
PF00045 Hemopexin, 4 hits
PF00413 Peptidase_M10, 1 hit
PF01471 PG_binding_1, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF001191 Peptidase_M10A_matrix, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00138 MATRIXIN

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00120 HX, 4 hits
SM00235 ZnMc, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF47090 SSF47090, 1 hit
SSF50923 SSF50923, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00546 CYSTEINE_SWITCH, 1 hit
PS00024 HEMOPEXIN, 1 hit
PS51642 HEMOPEXIN_2, 4 hits
PS00142 ZINC_PROTEASE, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

P50281-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSPAPRPPRC LLLPLLTLGT ALASLGSAQS SSFSPEAWLQ QYGYLPPGDL 
        60         70         80         90        100
RTHTQRSPQS LSAAIAAMQK FYGLQVTGKA DADTMKAMRR PRCGVPDKFG 
       110        120        130        140        150
AEIKANVRRK RYAIQGLKWQ HNEITFCIQN YTPKVGEYAT YEAIRKAFRV 
       160        170        180        190        200
WESATPLRFR EVPYAYIREG HEKQADIMIF FAEGFHGDST PFDGEGGFLA 
       210        220        230        240        250
HAYFPGPNIG GDTHFDSAEP WTVRNEDLNG NDIFLVAVHE LGHALGLEHS 
       260        270        280        290        300
SDPSAIMAPF YQWMDTENFV LPDDDRRGIQ QLYGGESGFP TKMPPQPRTT 
       310        320        330        340        350
SRPSVPDKPK NPTYGPNICD GNFDTVAMLR GEMFVFKERW FWRVRNNQVM 
       360        370        380        390        400
DGYPMPIGQF WRGLPASINT AYERKDGKFV FFKGDKHWVF DEASLEPGYP 
       410        420        430        440        450
KHIKELGRGL PTDKIDAALF WMPNGKTYFF RGNKYYRFNE ELRAVDSEYP 
       460        470        480        490        500
KNIKVWEGIP ESPRGSFMGS DEVFTYFYKG NKYWKFNNQK LKVEPGYPKS 
       510        520        530        540        550
ALRDWMGCPS GGRPDEGTEE ETEVIIIEVD EEGGGAVSAA AVVLPVLLLL 
       560        570        580 
LVLAVGLAVF FFRRHGTPRR LLYCQRSLLD KV
Length:582
Mass (Da):65,894
Last modified:January 11, 2011 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i3722DE286A4BBCDE
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F8W1B7F8W1B7_HUMAN
Matrix metalloproteinase
MMP14
194Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
F8VP90F8VP90_HUMAN
Matrix metalloproteinase
MMP14
71Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti338E → K in BAA05519 (PubMed:8015608).Curated1
Sequence conflicti500S → P in CAA62432 (PubMed:8706726).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0210294A → T1 PublicationCorresponds to variant dbSNP:rs17882219Ensembl.1
Natural variantiVAR_0210306R → K1 PublicationCorresponds to variant dbSNP:rs17884647Ensembl.1
Natural variantiVAR_0210318P → S7 PublicationsCorresponds to variant dbSNP:rs1042703Ensembl.1
Natural variantiVAR_07056717T → R in WNCHRS; results in increased MMP14 proteosomal degradation and reduced protein localization to cell membrane. 1 PublicationCorresponds to variant dbSNP:rs587777039EnsemblClinVar.1
Natural variantiVAR_021032233I → V1 PublicationCorresponds to variant dbSNP:rs17884841Ensembl.1
Natural variantiVAR_021033273D → N1 PublicationCorresponds to variant dbSNP:rs1042704Ensembl.1
Natural variantiVAR_021034302R → W1 PublicationCorresponds to variant dbSNP:rs17884719Ensembl.1
Natural variantiVAR_021035355M → I1 PublicationCorresponds to variant dbSNP:rs17880989Ensembl.1
Natural variantiVAR_031267431R → H. Corresponds to variant dbSNP:rs3751489Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
D26512 mRNA Translation: BAA05519.1
X83535 mRNA Translation: CAA58519.1
Z48481 mRNA Translation: CAA88372.1
U41078 mRNA Translation: AAA83770.1
X90925 mRNA Translation: CAA62432.1
AK291325 mRNA Translation: BAF84014.1
AY795074 Genomic DNA Translation: AAV40837.1
AL135998 Genomic DNA No translation available.
BC064803 mRNA Translation: AAH64803.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS9577.1

Protein sequence database of the Protein Information Resource

More...PIRi		I38028

NCBI Reference Sequences

More...RefSeqi		NP_004986.1, NM_004995.3

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.2399

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000311852; ENSP00000308208; ENSG00000157227

Database of genes from NCBI RefSeq genomes

More...GeneIDi		4323

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:4323

UCSC genome browser

More...UCSCi		uc001whc.5 human

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

NIEHS-SNPs
Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D26512 mRNA Translation: BAA05519.1
X83535 mRNA Translation: CAA58519.1
Z48481 mRNA Translation: CAA88372.1
U41078 mRNA Translation: AAA83770.1
X90925 mRNA Translation: CAA62432.1
AK291325 mRNA Translation: BAF84014.1
AY795074 Genomic DNA Translation: AAV40837.1
AL135998 Genomic DNA No translation available.
BC064803 mRNA Translation: AAH64803.1
CCDSiCCDS9577.1
PIRiI38028
RefSeqiNP_004986.1, NM_004995.3
UniGeneiHs.2399

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BQQX-ray2.75M114-287[»]
1BUVX-ray2.75M114-287[»]
2MQSNMR-A316-511[»]
3C7XX-ray1.70A316-511[»]
3MA2X-ray2.05A/D112-292[»]
3X23X-ray2.40B563-582[»]
4P3CX-ray1.94M215-227[»]
4P3DX-ray1.95C/M215-227[»]
4QXUX-ray2.30K218-228[»]
5H0UX-ray2.24A116-285[»]
ProteinModelPortaliP50281
SMRiP50281
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110466, 20 interactors
CORUMiP50281
DIPiDIP-35111N
IntActiP50281, 43 interactors
MINTiP50281
STRINGi9606.ENSP00000308208

Chemistry databases

BindingDBiP50281
ChEMBLiCHEMBL3869
DrugBankiDB00786 Marimastat
GuidetoPHARMACOLOGYi1638

Protein family/group databases

MEROPSiM10.014

PTM databases

iPTMnetiP50281
PhosphoSitePlusiP50281
SwissPalmiP50281

Polymorphism and mutation databases

BioMutaiMMP14
DMDMi317373419

Proteomic databases

EPDiP50281
MaxQBiP50281
PaxDbiP50281
PeptideAtlasiP50281
PRIDEiP50281
ProteomicsDBi56213

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000311852; ENSP00000308208; ENSG00000157227
GeneIDi4323
KEGGihsa:4323
UCSCiuc001whc.5 human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		4323
DisGeNETi4323
EuPathDBiHostDB:ENSG00000157227.12

GeneCards: human genes, protein and diseases

More...GeneCardsi		MMP14

H-Invitational Database, human transcriptome db

More...H-InvDBi		HIX0202102
HGNCiHGNC:7160 MMP14
HPAiCAB009918
HPA051432
MalaCardsiMMP14
MIMi277950 phenotype
600754 gene
neXtProtiNX_P50281
OpenTargetsiENSG00000157227
Orphaneti85196 Nodulosis-arthropathy-osteolysis syndrome
3460 Torg-Winchester syndrome
PharmGKBiPA30872

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG1565 Eukaryota
ENOG410XQ5D LUCA
GeneTreeiENSGT00940000157808
HOGENOMiHOG000217928
HOVERGENiHBG052484
InParanoidiP50281
KOiK07763
OMAiNAVMFPW
OrthoDBiEOG091G03DP
PhylomeDBiP50281
TreeFamiTF352396

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000157227-MONOMER
BRENDAi3.4.24.80 2681
3.4.24.B5 2681
ReactomeiR-HSA-1442490 Collagen degradation
R-HSA-1474228 Degradation of the extracellular matrix
R-HSA-1592389 Activation of Matrix Metalloproteinases
SIGNORiP50281

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		MMP14 human
EvolutionaryTraceiP50281

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		MMP14

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		4323

Protein Ontology

More...PROi		PR:P50281

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000157227 Expressed in 191 organ(s), highest expression level in endocervix
CleanExiHS_MMP14
ExpressionAtlasiP50281 baseline and differential
GenevisibleiP50281 HS

Family and domain databases

CDDicd00094 HX, 1 hit
cd04278 ZnMc_MMP, 1 hit
Gene3Di1.10.101.10, 1 hit
2.110.10.10, 1 hit
3.40.390.10, 1 hit
InterProiView protein in InterPro
IPR000585 Hemopexin-like_dom
IPR036375 Hemopexin-like_dom_sf
IPR018487 Hemopexin-like_repeat
IPR018486 Hemopexin_CS
IPR033739 M10A_MMP
IPR024079 MetalloPept_cat_dom_sf
IPR028693 MMP14
IPR001818 Pept_M10_metallopeptidase
IPR021190 Pept_M10A
IPR021805 Pept_M10A_metallopeptidase_C
IPR021158 Pept_M10A_Zn_BS
IPR006026 Peptidase_Metallo
IPR002477 Peptidoglycan-bd-like
IPR036365 PGBD-like_sf
IPR036366 PGBDSf
PANTHERiPTHR10201:SF24 PTHR10201:SF24, 1 hit
PfamiView protein in Pfam
PF11857 DUF3377, 1 hit
PF00045 Hemopexin, 4 hits
PF00413 Peptidase_M10, 1 hit
PF01471 PG_binding_1, 1 hit
PIRSFiPIRSF001191 Peptidase_M10A_matrix, 1 hit
PRINTSiPR00138 MATRIXIN
SMARTiView protein in SMART
SM00120 HX, 4 hits
SM00235 ZnMc, 1 hit
SUPFAMiSSF47090 SSF47090, 1 hit
SSF50923 SSF50923, 1 hit
PROSITEiView protein in PROSITE
PS00546 CYSTEINE_SWITCH, 1 hit
PS00024 HEMOPEXIN, 1 hit
PS51642 HEMOPEXIN_2, 4 hits
PS00142 ZINC_PROTEASE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiMMP14_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P50281
Secondary accession number(s): A8K5L0, Q6GSF3, Q92678
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 11, 2011
Last modified: December 5, 2018
This is version 197 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  4. Peptidase families
    Classification of peptidase families and list of entries
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  7. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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